STAD1_OPHSP
ID STAD1_OPHSP Reviewed; 378 AA.
AC E3PZS1;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Palmitoyl-[acyl-carrier-protein] 4-desaturase 1, chloroplastic;
DE EC=1.14.19.11 {ECO:0000250|UniProtKB:E3PZS2};
DE AltName: Full=Acyl-[acyl-carrier-protein] desaturase 1;
DE AltName: Full=Stearoyl-[acyl-carrier-protein] 9-desaturase 1;
DE Short=Stearoyl-ACP desaturase 1;
DE EC=1.14.19.2 {ECO:0000250|UniProtKB:E3PZS2};
DE Flags: Precursor;
GN Name=SAD1;
OS Ophrys sphegodes (Early spider orchid) (Arachnites aranifera).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC Orchidoideae; Orchideae; Orchidinae; Ophrys.
OX NCBI_TaxID=145953;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Flower;
RX PubMed=21436056; DOI=10.1073/pnas.1013313108;
RA Schlueter P.M., Xu S., Gagliardini V., Whittle E., Shanklin J.,
RA Grossniklaus U., Schiestl F.P.;
RT "Stearoyl-acyl carrier protein desaturases are associated with floral
RT isolation in sexually deceptive orchids.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:5696-5701(2011).
CC -!- FUNCTION: Converts stearoyl-ACP to oleoyl-ACP by introduction of a cis
CC double bond between carbons 9 and 10 of the acyl chain. Converts
CC palmitoyl-ACP to (4Z)-hexadec-4-enoyl-ACP by introduction of a cis
CC double bond between carbons 4 and 5 of the acyl chain.
CC {ECO:0000250|UniProtKB:E3PZS2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + hexadecanoyl-[ACP] + O2 + 2 reduced [2Fe-2S]-
CC [ferredoxin] = (4Z)-hexadecenoyl-[ACP] + 2 H2O + 2 oxidized [2Fe-2S]-
CC [ferredoxin]; Xref=Rhea:RHEA:38043, Rhea:RHEA-COMP:9652, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:11488,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:78483,
CC ChEBI:CHEBI:85919; EC=1.14.19.11;
CC Evidence={ECO:0000250|UniProtKB:E3PZS2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + O2 + octadecanoyl-[ACP] + 2 reduced [2Fe-2S]-
CC [ferredoxin] = (9Z)-octadecenoyl-[ACP] + 2 H2O + 2 oxidized [2Fe-2S]-
CC [ferredoxin]; Xref=Rhea:RHEA:11776, Rhea:RHEA-COMP:9656, Rhea:RHEA-
CC COMP:9924, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:78495,
CC ChEBI:CHEBI:78783; EC=1.14.19.2;
CC Evidence={ECO:0000250|UniProtKB:E3PZS2};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:P22337};
CC Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000250|UniProtKB:P22337};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P22337}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000250|UniProtKB:P22337}.
CC -!- TISSUE SPECIFICITY: Preferentially expressed in the flower labellum.
CC {ECO:0000269|PubMed:21436056}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 2 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FR688108; CBW95565.1; -; mRNA.
DR AlphaFoldDB; E3PZS1; -.
DR SMR; E3PZS1; -.
DR UniPathway; UPA00199; -.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0045300; F:acyl-[acyl-carrier-protein] desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0102786; F:stearoyl-[acp] desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd01050; Acyl_ACP_Desat; 1.
DR Gene3D; 1.10.620.20; -; 1.
DR InterPro; IPR005067; Fatty_acid_desaturase-2.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR012348; RNR-like.
DR PANTHER; PTHR31155; PTHR31155; 1.
DR Pfam; PF03405; FA_desaturase_2; 1.
DR PIRSF; PIRSF000346; Dlt9_acylACP_des; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Fatty acid biosynthesis; Fatty acid metabolism; Iron;
KW Lipid biosynthesis; Lipid metabolism; Metal-binding; Oxidoreductase;
KW Plastid; Transit peptide.
FT TRANSIT 1..23
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 24..378
FT /note="Palmitoyl-[acyl-carrier-protein] 4-desaturase 1,
FT chloroplastic"
FT /id="PRO_0000417063"
FT BINDING 116
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 151
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 151
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 154
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 204
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 237
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 237
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 240
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
SQ SEQUENCE 378 AA; 42705 MW; 36471DD7A7EFF4F7 CRC64;
MELHLALLAS PLPAAPGRRS LPRSSFATNS TTTINQTHLS PEKQEKLQSL LDTWAEHNLL
TFLKPVEKCW QPQDFLPDPS HLSPTELGDA VREIQERAAE IPDDVWVCMV GNMVTEEALP
TYQSMMSLVL GGTGADSNPW ERWIRGWSAE ENRHGDLLNK YLYLTGRLDM RQVEKTIQYL
IGAGMDIGVD NNALCGIIYA CFQEKATFIS HGNTARLANH HGDTALAKIC GLVAADEKRH
AAAYTNLMRK LFEVDPNESM MAFAHVMQAR VTMPASRMFD GRDPRLFTHF SDVSQKIGVY
TVGDYSEMLE FFLKEWDISD VVDGLSPEGR RAQEYVCGLP EVMRKLAERA DDRRKKLVNA
GEPRYIPFSW IFNKQVRV
